UFMylation: A supervisor of the HIF1α pathway and a potential therapeutic target for anti-PD-1 combination therapy in hypoxic tumors

Y Yongkang Zou (Institute of Cancer Research, Shenzhen Bay Laboratory) Z Zhaoxiang Wang (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University) Q Qiang Jiang (Department of Animal Genetics, College of Animal Science and Technology, Nanjing Agricultural University) X Xia Kong (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University) X Xiaohe Ma Z Zhengyan Liang (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University) Z Zhiguo Wang (Department of Cell Biology, School of Basic Medicine, Hangzhou Normal University) B Beiying Chen (Department of Cell Biology, School of Basic Medicine, Hangzhou Normal University) J Jiao Yuan (Guangzhou Medical University-Guangzhou Institutes of Biomedicine and Health Joint School of Life Sciences, The Guangdong-Hong Kong-Macao Joint Laboratory for Cell Fate Regulation and Diseases, Guangzhou Laboratory, Guangzhou Medical University) J Jiayue Wen (Guangzhou Medical University-Guangzhou Institutes of Biomedicine and Health Joint School of Life Sciences, The Guangdong-Hong Kong-Macao Joint Laboratory for Cell Fate Regulation and Diseases, Guangzhou Laboratory, Guangzhou Medical University) S Sheng Ye (School of Artificial Intelligence) Y Yubin Yan (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University) B Binbin Li (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University) X Xing-dong Xiong (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University) X Xin-guang Liu (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University) Z Zhiwei He (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University) Y Yafei Cai (Department of Animal Genetics, College of Animal Science and Technology, Nanjing Agricultural University) J Junzhi Zhou (Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University)

Abstract

Activation of hypoxia signaling has been identified as an innate resistance signature against anti-PD-1 therapy, suggesting its potential as a target for combination treatments. Here, we demonstrate that UFMylation modification of HIF1α stabilizes the protein by antagonizing its ubiquitination and proteasomal degradation under hypoxic conditions. Mechanistically, depletion of UFL1 or defective UFMylation increases HIF1α binding to p53, promoting its degradation. Depletion of UFL1 or UBA5 , or defective UFMylation of HIF1α, destabilizes HIF1α, significantly inhibiting tumor growth and development in vitro and in xenograft mouse models. Defective UFMylation of HIF1α enhances the response to anti-PD-1 therapy in xenograft models. Clinically, UBA5 expression is upregulated in breast cancer tissues, and a selective UBA5 inhibitor reduces UFMylation activity and HIF1α protein levels, thereby enhancing anti-PD-1 combination therapy in mouse tumor models. Our findings highlight UFMylation as a critical posttranslational modification for the HIF1α pathway and a promising therapeutic target in hypoxic tumors.

Article Details

Volume / Issue Vol. 122, Issue 27
Published July 08, 2025
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (18)

Y

Yongkang Zou

Institute of Cancer Research, Shenzhen Bay Laboratory

Z

Zhaoxiang Wang

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University

Q

Qiang Jiang

Department of Animal Genetics, College of Animal Science and Technology, Nanjing Agricultural University

X

Xia Kong

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University

X

Xiaohe Ma

Z

Zhengyan Liang

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University

Z

Zhiguo Wang

Department of Cell Biology, School of Basic Medicine, Hangzhou Normal University

B

Beiying Chen

Department of Cell Biology, School of Basic Medicine, Hangzhou Normal University

J

Jiao Yuan

Guangzhou Medical University-Guangzhou Institutes of Biomedicine and Health Joint School of Life Sciences, The Guangdong-Hong Kong-Macao Joint Laboratory for Cell Fate Regulation and Diseases, Guangzhou Laboratory, Guangzhou Medical University

J

Jiayue Wen

Guangzhou Medical University-Guangzhou Institutes of Biomedicine and Health Joint School of Life Sciences, The Guangdong-Hong Kong-Macao Joint Laboratory for Cell Fate Regulation and Diseases, Guangzhou Laboratory, Guangzhou Medical University

S

Sheng Ye

School of Artificial Intelligence

Y

Yubin Yan

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University

B

Binbin Li

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University

X

Xing-dong Xiong

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University

X

Xin-guang Liu

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University

Z

Zhiwei He

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University

Y

Yafei Cai

Department of Animal Genetics, College of Animal Science and Technology, Nanjing Agricultural University

J

Junzhi Zhou

Department of Pathophysiology, School of Basic Medicine, Key Laboratory for Epigenetics of Dongguan City, Guangdong Provincial Key Laboratory of Medical Immunology and Molecular Diagnostics, Guangdong Medical University